1887

Abstract

Summary: 1 is a facultative methylotroph which grows on a wide range of carbon compounds. A mutant of 1 (41) grew only on C compounds and is thus an artificial obligate methylotroph. Measurements of activities of the components of the 2-oxoglutarate dehydrogenase complex suggest that the E component (dihydrolipoamide transsuccinylase) is not functional. All other tricarboxylic acid cycle enzymes were present with activities comparable to those in wild-type 1 and cytochrome levels were unchanged in the mutant. Suspensions of the mutant oxidized pyruvate, lactate, -hydroxybutyrate, acetoacetate and 2-oxoglutarate at very low rates. By contrast, C compounds were oxidized at the same rate as in wild-type bacteria. Two revertants of 41 which regained 2-oxoglutarate dehydrogenase activity also regained the ability to oxidize and grow on the same substrates as wild-type bacteria. It is concluded that lack of 2-oxoglutarate dehydrogenase may well be the basis of obligate methylotrophy in some bacteria.

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1976-04-01
2022-01-22
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References

  1. Anthony C. 1975a; The biochemistry of methylotrophic micro-organisms. Science Progress (Oxford) 62:167–206
    [Google Scholar]
  2. Anthony C. 1975b; The microbial metabolism of C1 compounds: the cytochromes ofPseudomonas am1 . Biochemical Journal 146:289–298
    [Google Scholar]
  3. Blackmore M.A., Quayle J.R. 1970; Microbial growth on oxalate by a route not involving glyoxylate carboligase. Biochemical Journal 118:53–59
    [Google Scholar]
  4. Colby J., Zatman L.J. 1972; Hexose phosphate synthase and TCA cycle enzymes in bacterium 4b6, an obligate methylotroph. Biochemical Journal 128:1373–1376
    [Google Scholar]
  5. Colby J., Zatman L.J. 1975; Tricarboxylic acid-cycle and related enzymes in restricted facultative methylotrophs. Biochemical Journal 148:505–511
    [Google Scholar]
  6. Cox G.F. 1969; Isocitrate dehydrogenase (NAD-specific). In Methods in Enzymology 13: pp. 47–51 Lowenstein J. M. Edited by New York and London: Academic Press;
    [Google Scholar]
  7. Dahl J.S., Mehta R.J., Hoare D.S. 1972; New obligate methylotroph. Journal of Bacteriology 109:916–921
    [Google Scholar]
  8. Davey J.F., Whittenbury R., Wilkinson J.F. 1972; The distribution in the methylobacteria of some key enzymes concerned with intermediary metabolism. Archives of Microbiology 87:359–366
    [Google Scholar]
  9. Guest J.R., Creaghan I.T. 1973; Gene-protein relationships of the α-keto acid dehydrogenase complexes ofEscherichia coli k12: isolation and characterization of lipoamide dehydrogenase mutants. Journal of General Microbiology 75:197–210
    [Google Scholar]
  10. Hager L.P., Kornberg H.L. 1961; On the mechanism of α-oxoglutarate oxidation inEscherichia coli. Biochemical Journal 78:194–198
    [Google Scholar]
  11. Harder W., Martin A., Attwood M.M. 1975; Studies on the physiological significance of the lack of a pyruvate dehydrogenase complex inHyphomicrobium sp. Journal of General Microbiology 86:319–326
    [Google Scholar]
  12. Heptinstall J., Quayle J. R. Edited by 1970; Pathways leading to and from serine during growth of Pseudomonas ami on C1 compounds or succinate. Biochemical Journal 117:563–572
    [Google Scholar]
  13. Jones M.E., Lipmann F. 1955; Aceto-CoA-kinase. In Methods in Enzymology I: pp. 585–590 Colowick S. P., Kaplan. N. O. Edited by New York: Academic Press;
    [Google Scholar]
  14. Kaufmann S. 1955; P-enzyme. In Methods of Enzymology 1: pp. 718–722 Colowick S. P., Kaplan N. O. Edited by New York: Academic Press;
    [Google Scholar]
  15. Kelly D.P. 1971; Autotrophy: concepts of lithotrophic bacteria and their organic metabolism. Annual Review of Microbiology 25:177–210
    [Google Scholar]
  16. Massey V. 1966; Lipoyl dehydrogenase from pig heart. In Methods in Enzymology 9: pp. 272–278 Wood W. A. Edited by New York and London: Academic Press;
    [Google Scholar]
  17. Ochoa S. 1955a; Isocitrate dehydrogenase (NAD-specific). In Methods in Enzymology 1: pp. 699–704 Colowick S. P., Kaplan. N. O. Edited by New York: Academic Press;
    [Google Scholar]
  18. Ochoa S. 1955b; Malic dehydrogenase from pig heart. In Methods in Enzymology 1: pp. 735–739 Colowick S. P., Kaplan. N. O. Edited by New York: Academic Press;
    [Google Scholar]
  19. Quayle J.R. 1972; Metabolism of one-carbon compounds by micro-organisms. Advances in Microbial Physiology 7:119–197
    [Google Scholar]
  20. Racker E. 1950; Spectrophotometric measurements of the enzymatic formation of fumaric and cisaconitic acids. Biochimica et biophysica acta 4:211–215
    [Google Scholar]
  21. Reed L.J., Cox D.J. 1970; Multienzyme complexes. In The Enzymes, 3. I: pp. 213–240 Boyer. P. D. Edited by New York and London: Academic Press;
    [Google Scholar]
  22. Ribbons D.W., Harrison J.E., Wadzinski A.M. 1970; Metabolism of single carbon compounds. Annual Review of Microbiology 24:135–158
    [Google Scholar]
  23. Srere P.A. 1969; Citrate synthase. In Methods in Enzymology 12: pp. 3–11 Lowenstein J. M. Edited by New York and London: Academic Press;
    [Google Scholar]
  24. Veeger C., Der Vartanian D.V., Zeylemaker W.P. 1969; Succinate dehydrogenase. In Methods in Enzymology 13: pp. 81–90 Lowenstein J. M. Edited by New York and London: Academic Press;
    [Google Scholar]
  25. Widdowson D., Anthony C. 1975; The microbial metabolism of C1 compounds: the electron transport chain ofPseudomonasam1 . Biochemical Journal 152:349–356
    [Google Scholar]
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